Distribution of iron in six fractions (water-soluble, water-insoluble, diffusate, hematin, total heme, and ferritin) of beef and chicken muscles hcatcd to 55, 70, 85, and 100°C was determined. Iron content decreased in water-soluble fractions and increased in water-insoluble fractions as temperature increased from 27°C to 100°C. Heme iron decreased more from 55°C to 85°C than from 27°C to 55°C or 85°C to 100°C. The increase in diffusate iron appeared to be less than the decrease in heme iron at each heating temperature. As temperature increased from 27°C to IOtYC, hematin iron content increased and extractable ferritin iron content decreased. These findings may help explain rapid development of oxidative rancidity in cooked meat.

A flagellar sheath protein of Vibrio cholerae CA401 (Inaba) was characterized. Purity of the preparation was indicated by a single band on polyacrylamide gel electrophoresis gels and on Ouchterlony plates prepared with antibody against crude sheath material. The sheath protein was composed of three polypeptides with minimal molecular weights of 61,500, 60,000, and 56,500. The presence of sheath protein on the flagellum as well as on the outer membrane of the cell was demonstrated by ferritin labeling experiments with antiserum. Sheath protein antibody reacted similarly in labeling experiments and agglutination tests with a classical Ogawa strain and two nonagglutinating V. cholerae isolates, indicating that the sheath protein may represent the common Vibrio H antigen. Antibody specific for lipopolysaccharide labeled the cell but not the sheathed flagellum, which demonstrated that the sheath is not a simple extension of the outer membrane of the cell.

Corynebacterium nephridii was found to reduce nitrate (contrary to the original description) at a rapid rate. In the conventional 0.1% nitrate broth, neither nitrite nor nitrate was detected after 24 hr. There was no assimilation of nitrate nitrogen, and the final product of nitrate reduction was nitrous oxide. Manometric studies and growth experiments indicated that the organism is incapable of reducing nitrous oxide. C. nephridii is gram-negative, grows on bile salts (5%) agar, EMB Agar, and MacConkey Agar. It was proposed that this species be transferrrd to the genus Achromobacter and designated Achromobacter nephridii (Bulsing, D611, and Freytag) comb. nov.

Catalytic effects of different temperatures (55, 70, 85, and 100°C) on lipid oxidation were studied in aqueous-and chloroform/methanol-extracted beef model lipid systems containing iron forms inherent in beef (water-extractable, diffusate, nondiffusate, ferritin, myoglobin, hemoglobin), hematin, FeCl,, or FeCl,. Heating increased thiobarbituric acid and peroxide values in both systems. All forms of iron catalyzed lipid oxidation in aqueous systems, with greatest oxidation by heme and low molecular weight iron fractions. Oxidation in lipid extracts was not increased by ferritin, FeCl,, or FeCl,, but heme iron was the major oxidation catalyst. Lipid stability decreased with addition of any iron forms inherent in beef or with increased heating, which helps understanding of rapid oxidation of meat during refrigerated storage or after cooking.

The costa is an intracellular organelle common to all trichomonads. Costae from Tritrichomonas foetus have been purified by a method which involves lysis of T. foetus with the heat-stable hemolysin produced by Pseudomonas aeruginosa, followed by differential centrifugation. Analysis of the purified costae demonstrated that the organelle is composed of 95 percent carbohydrate and 5 percent protein. The carbohydrate moiety, probably a polysaccharide, consisted of glucose (95 percent), mannose (0.4 percent), glucosamine (1.4 percent), ribose (0.6 percent), and an unidentified sugar (2.6 percent). The kinetosomal complex was attached to the costa after initial lysis of cells but was separated from the costa during purification.